Studies on glutamic acid decarboxylase from Listeria monocytogenes.
The isolation and characterization of glutamic acid decarboxylase from Listeria monocytogenes has been described. Effects of various concentrations of glutamic acid as a substrate and pyridoxal phosphate as coenzyme on the activity of the partially purified enzyme have been examined and their Km and Vmax values determined. The enzyme exhibits relatively higher activity in 0.1 M pyridine-pyridine hydrochloride buffer with a pH value of 4.6.
D002021:Buffers; D002262:Carboxy-Lyases / Q000378:metabolism*; D005968:Glutamate Decarboxylase / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008089:Listeria monocytogenes / Q000201:enzymology*; D011725:Pyridines; D011732:Pyridoxal Phosphate / Q000378:metabolism; D012970:Sodium Glutamate / Q000378:metabolism
D002021:Buffers; D011725:Pyridines; D011732:Pyridoxal Phosphate; D002262:Carboxy-Lyases; D005968:Glutamate Decarboxylase; D012970:Sodium Glutamate